The LC Domain of hnRNPA2 Adopts Similar Conformations in Hydrogel Polymers, Liquid-like Droplets, and Nuclei

Siheng Xiang, Masato Kato, Leeju C. Wu, Yi Lin, Ming Ding, Yajie Zhang, Yonghao Yu, Steven L. McKnight

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110 Scopus citations


Many DNA and RNA regulatory proteins contain polypeptide domains that are unstructured when analyzed in cell lysates. These domains are typified by an over-representation of a limited number of amino acids and have been termed prion-like, intrinsically disordered or low-complexity (LC) domains. When incubated at high concentration, certain of these LC domains polymerize into labile, amyloid-like fibers. Here, we report methods allowing the generation of a molecular footprint of the polymeric state of the LC domain of hnRNPA2. By deploying this footprinting technique to probe the structure of the native hnRNPA2 protein present in isolated nuclei, we offer evidence that its LC domain exists in a similar conformation as that described for recombinant polymers of the protein. These observations favor biologic utility to the polymerization of LC domains in the pathway of information transfer from gene to message to protein.

Original languageEnglish (US)
Pages (from-to)829-839
Number of pages11
Issue number4
Publication statusPublished - Nov 5 2015


ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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